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LongText Report for: 6kf5-pdb

Name Class
6kf5-pdb
HEADER    HYDROLASE                               06-JUL-19   6KF5              
TITLE     MICROBIAL HORMONE-SENSITIVE LIPASE E53 MUTANT I256L                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LIPASE;                                                    
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ERYTHROBACTER LONGUS;                           
SOURCE   3 ORGANISM_TAXID: 1044;                                                
SOURCE   4 GENE: EH31_02760;                                                    
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';        
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 866768                                      
KEYWDS    ESTERASE, MICROBIAL HORMONE-SENSITIVE LIPASE, HYDROLASE               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.YANG,Z.Y.LI,J.LI,X.W.XU                                             
REVDAT   1   08-JUL-20 6KF5    0                                                
JRNL        AUTH   X.YANG,H.YINGYI,Z.Y.LI,J.SHULING,R.ZHEN,W.ZHAO,H.XIAOJIAN,   
JRNL        AUTH 2 C.HENGLIN,J.LI,X.W.XU                                        
JRNL        TITL   MICROBIAL HORMONE-SENSITIVE LIPASE E53 MUTANT I256L          
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.09 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.09                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.50                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 119096                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.184                           
REMARK   3   R VALUE            (WORKING SET) : 0.183                           
REMARK   3   FREE R VALUE                     : 0.214                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.930                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5874                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 19.5000 -  6.4300    0.95     3857   203  0.2128 0.2150        
REMARK   3     2  6.4300 -  5.1300    0.99     3927   179  0.2038 0.2344        
REMARK   3     3  5.1300 -  4.4900    1.00     3854   192  0.1611 0.1798        
REMARK   3     4  4.4900 -  4.0900    1.00     3845   192  0.1539 0.1742        
REMARK   3     5  4.0900 -  3.8000    1.00     3824   197  0.1592 0.2057        
REMARK   3     6  3.8000 -  3.5700    1.00     3798   210  0.1747 0.2002        
REMARK   3     7  3.5700 -  3.4000    1.00     3772   203  0.1715 0.2160        
REMARK   3     8  3.4000 -  3.2500    1.00     3803   209  0.1814 0.1815        
REMARK   3     9  3.2500 -  3.1200    1.00     3831   177  0.1809 0.2283        
REMARK   3    10  3.1200 -  3.0200    1.00     3791   171  0.1852 0.2278        
REMARK   3    11  3.0200 -  2.9200    1.00     3800   189  0.1764 0.1961        
REMARK   3    12  2.9200 -  2.8400    1.00     3764   199  0.1841 0.2367        
REMARK   3    13  2.8400 -  2.7600    1.00     3804   194  0.1764 0.2092        
REMARK   3    14  2.7600 -  2.7000    1.00     3781   189  0.1776 0.1940        
REMARK   3    15  2.7000 -  2.6400    1.00     3713   224  0.1810 0.2192        
REMARK   3    16  2.6400 -  2.5800    1.00     3790   198  0.1806 0.2088        
REMARK   3    17  2.5800 -  2.5300    1.00     3776   164  0.1812 0.2185        
REMARK   3    18  2.5300 -  2.4800    1.00     3794   184  0.1869 0.2521        
REMARK   3    19  2.4800 -  2.4400    1.00     3720   197  0.1877 0.2164        
REMARK   3    20  2.4400 -  2.4000    1.00     3770   214  0.1912 0.2316        
REMARK   3    21  2.4000 -  2.3600    1.00     3701   195  0.1842 0.2050        
REMARK   3    22  2.3600 -  2.3200    1.00     3805   186  0.1911 0.2291        
REMARK   3    23  2.3200 -  2.2900    1.00     3704   210  0.1893 0.2446        
REMARK   3    24  2.2900 -  2.2500    1.00     3754   200  0.1971 0.2560        
REMARK   3    25  2.2500 -  2.2200    1.00     3702   219  0.2012 0.2620        
REMARK   3    26  2.2200 -  2.2000    1.00     3742   194  0.2038 0.2447        
REMARK   3    27  2.2000 -  2.1700    1.00     3740   181  0.2062 0.2493        
REMARK   3    28  2.1700 -  2.1400    1.00     3708   197  0.2166 0.2354        
REMARK   3    29  2.1400 -  2.1200    1.00     3751   202  0.2282 0.2656        
REMARK   3    30  2.1200 -  2.0900    0.97     3601   205  0.2325 0.2792        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.204            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.399           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 27.23                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.79                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007           9438                                  
REMARK   3   ANGLE     :  0.878          12853                                  
REMARK   3   CHIRALITY :  0.053           1475                                  
REMARK   3   PLANARITY :  0.006           1701                                  
REMARK   3   DIHEDRAL  :  5.624           5681                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6KF5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-JUL-19.                  
REMARK 100 THE DEPOSITION ID IS D_1300012863.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-MAY-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 80                                 
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL19U1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97776                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 119275                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.090                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 13.10                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 17.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.09                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.13                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4YPV                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.31                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.88                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CALCIUM CHLORIDE, BIS-TRIS, PEG MME      
REMARK 280  550, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 2 21                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,-Y,-Z+1/2                                         
REMARK 290       4555   -X+1/2,-Y,Z+1/2                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       35.38600            
REMARK 290   SMTRY2   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      109.85350            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       35.38600            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      109.85350            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B 718  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 730  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     THR A   313                                                      
REMARK 465     ALA A   314                                                      
REMARK 465     MET B     1                                                      
REMARK 465     THR B     2                                                      
REMARK 465     ASP B     3                                                      
REMARK 465     THR B   313                                                      
REMARK 465     ALA B   314                                                      
REMARK 465     MET C     1                                                      
REMARK 465     THR C     2                                                      
REMARK 465     ASP C     3                                                      
REMARK 465     THR C   313                                                      
REMARK 465     ALA C   314                                                      
REMARK 465     MET D     1                                                      
REMARK 465     THR D     2                                                      
REMARK 465     ASP D     3                                                      
REMARK 465     GLU D    79                                                      
REMARK 465     THR D   313                                                      
REMARK 465     ALA D   314                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     THR A   4    OG1  CG2                                            
REMARK 470     GLU A  79    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 178    CG   CD   CE   NZ                                   
REMARK 470     THR B   4    OG1  CG2                                            
REMARK 470     GLU B  32    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  76    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 178    CG   CD   CE   NZ                                   
REMARK 470     THR C   4    OG1  CG2                                            
REMARK 470     GLU C  76    CG   CD   OE1  OE2                                  
REMARK 470     GLU C  79    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 178    CG   CD   CE   NZ                                   
REMARK 470     THR D   4    OG1  CG2                                            
REMARK 470     LYS D 178    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   690     O    HOH A   754              2.00            
REMARK 500   O    HOH A   623     O    HOH A   650              2.06            
REMARK 500   OE2  GLU D    16     O    HOH D   501              2.06            
REMARK 500   O    HOH A   730     O    HOH A   738              2.13            
REMARK 500   O    HOH C   619     O    HOH C   701              2.14            
REMARK 500   O    HOH C   686     O    HOH C   762              2.15            
REMARK 500   O    HOH C   616     O    HOH C   721              2.15            
REMARK 500   O    HOH D   619     O    HOH D   700              2.17            
REMARK 500   O    HOH B   673     O    HOH B   679              2.17            
REMARK 500   O    HOH D   639     O    HOH D   712              2.18            
REMARK 500   OE2  GLU C   133     O    HOH C   501              2.18            
REMARK 500   O    HOH A   778     O    HOH C   761              2.18            
REMARK 500   O    HOH A   650     O    HOH A   710              2.18            
REMARK 500   O    GLU B    33     O    HOH B   501              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH D   501     O    HOH D   501     2754     1.89            
REMARK 500   O    HOH D   502     O    HOH D   502     2754     1.93            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  96     -160.49   -164.37                                   
REMARK 500    SER A 162     -117.02     68.17                                   
REMARK 500    LEU A 186      142.41   -170.53                                   
REMARK 500    PHE A 191       65.61     20.05                                   
REMARK 500    VAL A 211      -70.25     69.21                                   
REMARK 500    ASP B  96     -159.89   -164.14                                   
REMARK 500    SER B 162     -113.96     61.96                                   
REMARK 500    PHE B 191       66.86     19.40                                   
REMARK 500    VAL B 211      -71.68     66.94                                   
REMARK 500    HIS B 284      147.61    -39.22                                   
REMARK 500    ALA C  22     -133.61     60.73                                   
REMARK 500    ASP C  96     -161.77   -162.52                                   
REMARK 500    PHE C 128      134.07    -39.53                                   
REMARK 500    PRO C 129       31.62    -99.12                                   
REMARK 500    SER C 162     -116.78     66.16                                   
REMARK 500    LEU C 186      140.10   -174.67                                   
REMARK 500    PHE C 191       63.08     21.90                                   
REMARK 500    VAL C 211      -73.61     69.99                                   
REMARK 500    HIS C 284      151.12    -42.78                                   
REMARK 500    ASP D  96     -161.03   -166.60                                   
REMARK 500    SER D 162     -111.92     65.62                                   
REMARK 500    LEU D 186      139.46   -174.18                                   
REMARK 500    PHE D 191       66.05     20.94                                   
REMARK 500    VAL D 211      -68.55     69.68                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 788        DISTANCE =  5.94 ANGSTROMS                       
REMARK 525    HOH A 789        DISTANCE =  6.07 ANGSTROMS                       
REMARK 525    HOH A 790        DISTANCE =  6.31 ANGSTROMS                       
REMARK 525    HOH A 791        DISTANCE =  6.38 ANGSTROMS                       
REMARK 525    HOH B 736        DISTANCE =  7.16 ANGSTROMS                       
REMARK 525    HOH D 721        DISTANCE =  6.06 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue D8F A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 6NA A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 2FK A 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue D8F B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue D8F C 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue D8F D 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 405                 
DBREF1 6KF5 A    1   314  UNP                  A0A074MDU6_ERYLO                 
DBREF2 6KF5 A     A0A074MDU6                          1         314             
DBREF1 6KF5 B    1   314  UNP                  A0A074MDU6_ERYLO                 
DBREF2 6KF5 B     A0A074MDU6                          1         314             
DBREF1 6KF5 C    1   314  UNP                  A0A074MDU6_ERYLO                 
DBREF2 6KF5 C     A0A074MDU6                          1         314             
DBREF1 6KF5 D    1   314  UNP                  A0A074MDU6_ERYLO                 
DBREF2 6KF5 D     A0A074MDU6                          1         314             
SEQADV 6KF5 LEU A  256  UNP  A0A074MDU ILE   256 ENGINEERED MUTATION            
SEQADV 6KF5 LEU B  256  UNP  A0A074MDU ILE   256 ENGINEERED MUTATION            
SEQADV 6KF5 LEU C  256  UNP  A0A074MDU ILE   256 ENGINEERED MUTATION            
SEQADV 6KF5 LEU D  256  UNP  A0A074MDU ILE   256 ENGINEERED MUTATION            
SEQRES   1 A  314  MET THR ASP THR PRO PHE ILE ARG PRO ASP MET LYS ALA          
SEQRES   2 A  314  PHE LEU GLU ALA ILE ALA ALA MET ALA GLY PRO THR LEU          
SEQRES   3 A  314  ALA GLU MET THR LEU GLU GLU ALA ARG ALA SER TYR VAL          
SEQRES   4 A  314  ALA LEU HIS GLY MET ALA ASP ARG PRO ALA ARG GLU LEU          
SEQRES   5 A  314  ALA VAL ILE ARG ASN LEU SER CYS PRO GLY PRO ALA GLY          
SEQRES   6 A  314  ASP ILE PRO LEU ARG LEU TYR ASP ALA ARG GLU SER ARG          
SEQRES   7 A  314  GLU ALA GLY PRO VAL ILE THR PHE TYR HIS GLY GLY GLY          
SEQRES   8 A  314  PHE VAL ILE GLY ASP LEU ASP THR HIS HIS ASN LEU CYS          
SEQRES   9 A  314  THR GLU ILE ALA ALA LEU MET ASP LEU PRO VAL VAL ALA          
SEQRES  10 A  314  VAL ASP TYR ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA          
SEQRES  11 A  314  ALA ILE GLU ASP CYS GLU ALA ALA THR ARG TRP VAL ALA          
SEQRES  12 A  314  SER SER PRO SER GLU LEU GLY ARG THR ALA SER GLY VAL          
SEQRES  13 A  314  ILE PRO ILE GLY ASP SER ALA GLY GLY ASN ALA THR ILE          
SEQRES  14 A  314  VAL VAL SER GLN LEU LEU GLY ALA LYS PRO ALA ASP VAL          
SEQRES  15 A  314  PRO VAL VAL LEU GLN VAL PRO ILE PHE PRO LEU ALA SER          
SEQRES  16 A  314  ASP ALA VAL GLY SER ALA SER LEU GLU ALA PHE ALA GLU          
SEQRES  17 A  314  GLY PHE VAL LEU THR LYS ALA SER ILE GLU PHE PHE ASP          
SEQRES  18 A  314  THR ALA TYR LYS ALA ASP ARG ALA ASP PRO ARG GLY PHE          
SEQRES  19 A  314  PRO ILE LEU GLY ASP HIS THR ALA ALA PRO PRO THR ILE          
SEQRES  20 A  314  VAL ALA THR ALA SER LEU ASP PRO LEU ARG ASP SER GLY          
SEQRES  21 A  314  ARG ASP TYR ALA LYS ALA LEU VAL GLU ALA GLY ARG ASP          
SEQRES  22 A  314  VAL VAL TYR LEU GLU MET GLU GLY VAL THR HIS SER PHE          
SEQRES  23 A  314  THR ASN ILE ARG ALA ALA VAL PRO SER THR GLN GLY ASP          
SEQRES  24 A  314  LEU GLU ARG ILE ILE ALA ALA MET LYS MET MET LEU GLY          
SEQRES  25 A  314  THR ALA                                                      
SEQRES   1 B  314  MET THR ASP THR PRO PHE ILE ARG PRO ASP MET LYS ALA          
SEQRES   2 B  314  PHE LEU GLU ALA ILE ALA ALA MET ALA GLY PRO THR LEU          
SEQRES   3 B  314  ALA GLU MET THR LEU GLU GLU ALA ARG ALA SER TYR VAL          
SEQRES   4 B  314  ALA LEU HIS GLY MET ALA ASP ARG PRO ALA ARG GLU LEU          
SEQRES   5 B  314  ALA VAL ILE ARG ASN LEU SER CYS PRO GLY PRO ALA GLY          
SEQRES   6 B  314  ASP ILE PRO LEU ARG LEU TYR ASP ALA ARG GLU SER ARG          
SEQRES   7 B  314  GLU ALA GLY PRO VAL ILE THR PHE TYR HIS GLY GLY GLY          
SEQRES   8 B  314  PHE VAL ILE GLY ASP LEU ASP THR HIS HIS ASN LEU CYS          
SEQRES   9 B  314  THR GLU ILE ALA ALA LEU MET ASP LEU PRO VAL VAL ALA          
SEQRES  10 B  314  VAL ASP TYR ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA          
SEQRES  11 B  314  ALA ILE GLU ASP CYS GLU ALA ALA THR ARG TRP VAL ALA          
SEQRES  12 B  314  SER SER PRO SER GLU LEU GLY ARG THR ALA SER GLY VAL          
SEQRES  13 B  314  ILE PRO ILE GLY ASP SER ALA GLY GLY ASN ALA THR ILE          
SEQRES  14 B  314  VAL VAL SER GLN LEU LEU GLY ALA LYS PRO ALA ASP VAL          
SEQRES  15 B  314  PRO VAL VAL LEU GLN VAL PRO ILE PHE PRO LEU ALA SER          
SEQRES  16 B  314  ASP ALA VAL GLY SER ALA SER LEU GLU ALA PHE ALA GLU          
SEQRES  17 B  314  GLY PHE VAL LEU THR LYS ALA SER ILE GLU PHE PHE ASP          
SEQRES  18 B  314  THR ALA TYR LYS ALA ASP ARG ALA ASP PRO ARG GLY PHE          
SEQRES  19 B  314  PRO ILE LEU GLY ASP HIS THR ALA ALA PRO PRO THR ILE          
SEQRES  20 B  314  VAL ALA THR ALA SER LEU ASP PRO LEU ARG ASP SER GLY          
SEQRES  21 B  314  ARG ASP TYR ALA LYS ALA LEU VAL GLU ALA GLY ARG ASP          
SEQRES  22 B  314  VAL VAL TYR LEU GLU MET GLU GLY VAL THR HIS SER PHE          
SEQRES  23 B  314  THR ASN ILE ARG ALA ALA VAL PRO SER THR GLN GLY ASP          
SEQRES  24 B  314  LEU GLU ARG ILE ILE ALA ALA MET LYS MET MET LEU GLY          
SEQRES  25 B  314  THR ALA                                                      
SEQRES   1 C  314  MET THR ASP THR PRO PHE ILE ARG PRO ASP MET LYS ALA          
SEQRES   2 C  314  PHE LEU GLU ALA ILE ALA ALA MET ALA GLY PRO THR LEU          
SEQRES   3 C  314  ALA GLU MET THR LEU GLU GLU ALA ARG ALA SER TYR VAL          
SEQRES   4 C  314  ALA LEU HIS GLY MET ALA ASP ARG PRO ALA ARG GLU LEU          
SEQRES   5 C  314  ALA VAL ILE ARG ASN LEU SER CYS PRO GLY PRO ALA GLY          
SEQRES   6 C  314  ASP ILE PRO LEU ARG LEU TYR ASP ALA ARG GLU SER ARG          
SEQRES   7 C  314  GLU ALA GLY PRO VAL ILE THR PHE TYR HIS GLY GLY GLY          
SEQRES   8 C  314  PHE VAL ILE GLY ASP LEU ASP THR HIS HIS ASN LEU CYS          
SEQRES   9 C  314  THR GLU ILE ALA ALA LEU MET ASP LEU PRO VAL VAL ALA          
SEQRES  10 C  314  VAL ASP TYR ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA          
SEQRES  11 C  314  ALA ILE GLU ASP CYS GLU ALA ALA THR ARG TRP VAL ALA          
SEQRES  12 C  314  SER SER PRO SER GLU LEU GLY ARG THR ALA SER GLY VAL          
SEQRES  13 C  314  ILE PRO ILE GLY ASP SER ALA GLY GLY ASN ALA THR ILE          
SEQRES  14 C  314  VAL VAL SER GLN LEU LEU GLY ALA LYS PRO ALA ASP VAL          
SEQRES  15 C  314  PRO VAL VAL LEU GLN VAL PRO ILE PHE PRO LEU ALA SER          
SEQRES  16 C  314  ASP ALA VAL GLY SER ALA SER LEU GLU ALA PHE ALA GLU          
SEQRES  17 C  314  GLY PHE VAL LEU THR LYS ALA SER ILE GLU PHE PHE ASP          
SEQRES  18 C  314  THR ALA TYR LYS ALA ASP ARG ALA ASP PRO ARG GLY PHE          
SEQRES  19 C  314  PRO ILE LEU GLY ASP HIS THR ALA ALA PRO PRO THR ILE          
SEQRES  20 C  314  VAL ALA THR ALA SER LEU ASP PRO LEU ARG ASP SER GLY          
SEQRES  21 C  314  ARG ASP TYR ALA LYS ALA LEU VAL GLU ALA GLY ARG ASP          
SEQRES  22 C  314  VAL VAL TYR LEU GLU MET GLU GLY VAL THR HIS SER PHE          
SEQRES  23 C  314  THR ASN ILE ARG ALA ALA VAL PRO SER THR GLN GLY ASP          
SEQRES  24 C  314  LEU GLU ARG ILE ILE ALA ALA MET LYS MET MET LEU GLY          
SEQRES  25 C  314  THR ALA                                                      
SEQRES   1 D  314  MET THR ASP THR PRO PHE ILE ARG PRO ASP MET LYS ALA          
SEQRES   2 D  314  PHE LEU GLU ALA ILE ALA ALA MET ALA GLY PRO THR LEU          
SEQRES   3 D  314  ALA GLU MET THR LEU GLU GLU ALA ARG ALA SER TYR VAL          
SEQRES   4 D  314  ALA LEU HIS GLY MET ALA ASP ARG PRO ALA ARG GLU LEU          
SEQRES   5 D  314  ALA VAL ILE ARG ASN LEU SER CYS PRO GLY PRO ALA GLY          
SEQRES   6 D  314  ASP ILE PRO LEU ARG LEU TYR ASP ALA ARG GLU SER ARG          
SEQRES   7 D  314  GLU ALA GLY PRO VAL ILE THR PHE TYR HIS GLY GLY GLY          
SEQRES   8 D  314  PHE VAL ILE GLY ASP LEU ASP THR HIS HIS ASN LEU CYS          
SEQRES   9 D  314  THR GLU ILE ALA ALA LEU MET ASP LEU PRO VAL VAL ALA          
SEQRES  10 D  314  VAL ASP TYR ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA          
SEQRES  11 D  314  ALA ILE GLU ASP CYS GLU ALA ALA THR ARG TRP VAL ALA          
SEQRES  12 D  314  SER SER PRO SER GLU LEU GLY ARG THR ALA SER GLY VAL          
SEQRES  13 D  314  ILE PRO ILE GLY ASP SER ALA GLY GLY ASN ALA THR ILE          
SEQRES  14 D  314  VAL VAL SER GLN LEU LEU GLY ALA LYS PRO ALA ASP VAL          
SEQRES  15 D  314  PRO VAL VAL LEU GLN VAL PRO ILE PHE PRO LEU ALA SER          
SEQRES  16 D  314  ASP ALA VAL GLY SER ALA SER LEU GLU ALA PHE ALA GLU          
SEQRES  17 D  314  GLY PHE VAL LEU THR LYS ALA SER ILE GLU PHE PHE ASP          
SEQRES  18 D  314  THR ALA TYR LYS ALA ASP ARG ALA ASP PRO ARG GLY PHE          
SEQRES  19 D  314  PRO ILE LEU GLY ASP HIS THR ALA ALA PRO PRO THR ILE          
SEQRES  20 D  314  VAL ALA THR ALA SER LEU ASP PRO LEU ARG ASP SER GLY          
SEQRES  21 D  314  ARG ASP TYR ALA LYS ALA LEU VAL GLU ALA GLY ARG ASP          
SEQRES  22 D  314  VAL VAL TYR LEU GLU MET GLU GLY VAL THR HIS SER PHE          
SEQRES  23 D  314  THR ASN ILE ARG ALA ALA VAL PRO SER THR GLN GLY ASP          
SEQRES  24 D  314  LEU GLU ARG ILE ILE ALA ALA MET LYS MET MET LEU GLY          
SEQRES  25 D  314  THR ALA                                                      
HET    D8F  A 401      17                                                       
HET    6NA  A 402       8                                                       
HET    EDO  A 403       4                                                       
HET    EDO  A 404       4                                                       
HET    GOL  A 405       6                                                       
HET    GOL  A 406       6                                                       
HET    2FK  A 407       2                                                       
HET    D8F  B 401      17                                                       
HET    GOL  B 402       6                                                       
HET    GOL  B 403       6                                                       
HET    D8F  C 401      17                                                       
HET    EDO  C 402       4                                                       
HET    D8F  D 401      17                                                       
HET    GOL  D 402       6                                                       
HET    GOL  D 403       6                                                       
HET    GOL  D 404       6                                                       
HET    GOL  D 405       6                                                       
HETNAM     D8F (4-NITROPHENYL) HEXANOATE                                        
HETNAM     6NA HEXANOIC ACID                                                    
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     GOL GLYCEROL                                                         
HETNAM     2FK SUPEROXO ION                                                     
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  D8F    4(C12 H15 N O4)                                              
FORMUL   6  6NA    C6 H12 O2                                                    
FORMUL   7  EDO    3(C2 H6 O2)                                                  
FORMUL   9  GOL    8(C3 H8 O3)                                                  
FORMUL  11  2FK    O2 1-                                                        
FORMUL  22  HOH   *1042(H2 O)                                                   
HELIX    1 AA1 ARG A    8  ALA A   22  1                                  15    
HELIX    2 AA2 THR A   25  MET A   29  5                                   5    
HELIX    3 AA3 THR A   30  ASP A   46  1                                  17    
HELIX    4 AA4 HIS A  100  ASP A  112  1                                  13    
HELIX    5 AA5 PRO A  129  SER A  144  1                                  16    
HELIX    6 AA6 SER A  145  GLY A  150  5                                   6    
HELIX    7 AA7 SER A  162  LYS A  178  1                                  17    
HELIX    8 AA8 SER A  200  PHE A  206  1                                   7    
HELIX    9 AA9 THR A  213  LYS A  225  1                                  13    
HELIX   10 AB1 PHE A  234  GLY A  238  5                                   5    
HELIX   11 AB2 LEU A  256  ALA A  270  1                                  15    
HELIX   12 AB3 SER A  285  ILE A  289  5                                   5    
HELIX   13 AB4 PRO A  294  GLY A  312  1                                  19    
HELIX   14 AB5 ARG B    8  ALA B   22  1                                  15    
HELIX   15 AB6 THR B   30  ASP B   46  1                                  17    
HELIX   16 AB7 HIS B  100  ASP B  112  1                                  13    
HELIX   17 AB8 PRO B  129  SER B  144  1                                  16    
HELIX   18 AB9 SER B  145  GLY B  150  5                                   6    
HELIX   19 AC1 SER B  162  LYS B  178  1                                  17    
HELIX   20 AC2 SER B  200  PHE B  206  1                                   7    
HELIX   21 AC3 THR B  213  LYS B  225  1                                  13    
HELIX   22 AC4 PHE B  234  GLY B  238  5                                   5    
HELIX   23 AC5 LEU B  256  ALA B  270  1                                  15    
HELIX   24 AC6 SER B  285  ILE B  289  5                                   5    
HELIX   25 AC7 SER B  295  GLY B  312  1                                  18    
HELIX   26 AC8 ARG C    8  ALA C   22  1                                  15    
HELIX   27 AC9 THR C   30  ASP C   46  1                                  17    
HELIX   28 AD1 HIS C  100  ASP C  112  1                                  13    
HELIX   29 AD2 PRO C  129  SER C  144  1                                  16    
HELIX   30 AD3 SER C  145  GLY C  150  5                                   6    
HELIX   31 AD4 SER C  162  LYS C  178  1                                  17    
HELIX   32 AD5 SER C  200  PHE C  206  1                                   7    
HELIX   33 AD6 THR C  213  LYS C  225  1                                  13    
HELIX   34 AD7 PHE C  234  GLY C  238  5                                   5    
HELIX   35 AD8 LEU C  256  ALA C  270  1                                  15    
HELIX   36 AD9 SER C  285  ILE C  289  5                                   5    
HELIX   37 AE1 PRO C  294  GLY C  312  1                                  19    
HELIX   38 AE2 ARG D    8  ALA D   22  1                                  15    
HELIX   39 AE3 THR D   30  ASP D   46  1                                  17    
HELIX   40 AE4 HIS D  100  ASP D  112  1                                  13    
HELIX   41 AE5 PRO D  129  SER D  144  1                                  16    
HELIX   42 AE6 SER D  145  GLY D  150  5                                   6    
HELIX   43 AE7 SER D  162  LYS D  178  1                                  17    
HELIX   44 AE8 SER D  200  PHE D  206  1                                   7    
HELIX   45 AE9 THR D  213  LYS D  225  1                                  13    
HELIX   46 AF1 PHE D  234  GLY D  238  5                                   5    
HELIX   47 AF2 LEU D  256  ALA D  270  1                                  15    
HELIX   48 AF3 SER D  285  ILE D  289  5                                   5    
HELIX   49 AF4 PRO D  294  GLY D  312  1                                  19    
SHEET    1 AA1 6 VAL A  54  GLY A  62  0                                        
SHEET    2 AA1 6 GLY A  65  ASP A  73 -1  O  LEU A  69   N  LEU A  58           
SHEET    3 AA1 6 VAL A 115  VAL A 118 -1  O  VAL A 115   N  TYR A  72           
SHEET    4 AA1 6 GLY A  81  TYR A  87  1  N  ILE A  84   O  VAL A 116           
SHEET    5 AA1 6 ALA A 153  ASP A 161  1  O  ILE A 157   N  VAL A  83           
SHEET    6 AA1 6 VAL A 188  ILE A 190  1  O  ILE A 190   N  GLY A 160           
SHEET    1 AA2 4 THR A 246  ALA A 251  0                                        
SHEET    2 AA2 4 VAL A 274  MET A 279  1  O  MET A 279   N  THR A 250           
SHEET    3 AA2 4 VAL B 274  MET B 279 -1  O  VAL B 274   N  TYR A 276           
SHEET    4 AA2 4 THR B 246  ALA B 251  1  N  THR B 250   O  LEU B 277           
SHEET    1 AA3 6 VAL B  54  CYS B  60  0                                        
SHEET    2 AA3 6 ILE B  67  ASP B  73 -1  O  ILE B  67   N  CYS B  60           
SHEET    3 AA3 6 VAL B 115  VAL B 118 -1  O  VAL B 115   N  TYR B  72           
SHEET    4 AA3 6 GLY B  81  TYR B  87  1  N  ILE B  84   O  VAL B 116           
SHEET    5 AA3 6 ALA B 153  ASP B 161  1  O  GLY B 155   N  VAL B  83           
SHEET    6 AA3 6 VAL B 188  ILE B 190  1  O  ILE B 190   N  GLY B 160           
SHEET    1 AA4 6 VAL C  54  CYS C  60  0                                        
SHEET    2 AA4 6 ILE C  67  ASP C  73 -1  O  LEU C  69   N  LEU C  58           
SHEET    3 AA4 6 VAL C 115  VAL C 118 -1  O  VAL C 115   N  TYR C  72           
SHEET    4 AA4 6 GLY C  81  TYR C  87  1  N  ILE C  84   O  VAL C 116           
SHEET    5 AA4 6 ALA C 153  ASP C 161  1  O  ILE C 157   N  VAL C  83           
SHEET    6 AA4 6 VAL C 188  ILE C 190  1  O  ILE C 190   N  GLY C 160           
SHEET    1 AA5 4 THR C 246  ALA C 251  0                                        
SHEET    2 AA5 4 VAL C 274  MET C 279  1  O  VAL C 275   N  VAL C 248           
SHEET    3 AA5 4 VAL D 274  MET D 279 -1  O  VAL D 274   N  TYR C 276           
SHEET    4 AA5 4 THR D 246  ALA D 251  1  N  THR D 250   O  LEU D 277           
SHEET    1 AA6 6 VAL D  54  CYS D  60  0                                        
SHEET    2 AA6 6 ILE D  67  ASP D  73 -1  O  LEU D  71   N  ARG D  56           
SHEET    3 AA6 6 VAL D 115  VAL D 118 -1  O  VAL D 115   N  TYR D  72           
SHEET    4 AA6 6 GLY D  81  TYR D  87  1  N  ILE D  84   O  VAL D 116           
SHEET    5 AA6 6 ALA D 153  ASP D 161  1  O  ILE D 157   N  VAL D  83           
SHEET    6 AA6 6 VAL D 188  ILE D 190  1  O  ILE D 190   N  GLY D 160           
CISPEP   1 ALA A  123    PRO A  124          0         0.86                     
CISPEP   2 PHE A  128    PRO A  129          0         3.57                     
CISPEP   3 ALA B  123    PRO B  124          0        -0.01                     
CISPEP   4 PHE B  128    PRO B  129          0         5.65                     
CISPEP   5 ALA C  123    PRO C  124          0         1.10                     
CISPEP   6 PHE C  128    PRO C  129          0         1.69                     
CISPEP   7 LEU C  311    GLY C  312          0         0.69                     
CISPEP   8 ALA D  123    PRO D  124          0         1.38                     
CISPEP   9 PHE D  128    PRO D  129          0         4.06                     
CISPEP  10 LEU D  311    GLY D  312          0       -13.18                     
SITE     1 AC1 14 TYR A  38  GLY A  90  GLY A  91  SER A 162                    
SITE     2 AC1 14 ALA A 163  LEU A 193  LEU A 212  ILE A 217                    
SITE     3 AC1 14 PHE A 220  HIS A 284  SER A 285  HOH A 529                    
SITE     4 AC1 14 HOH A 530  HOH A 637                                          
SITE     1 AC2  5 GLU A 136  LEU A 174  ARG A 232  HOH A 760                    
SITE     2 AC2  5 PRO C  63                                                     
SITE     1 AC3  8 ARG A  35  TYR A  38  VAL A  39  GLY A  95                    
SITE     2 AC3  8 ASP A  96  THR A  99  HOH A 559  HOH A 654                    
SITE     1 AC4  4 GLU A  51  LEU A  52  ILE A  55  HOH A 522                    
SITE     1 AC5  6 ARG A 257  ARG A 261  GOL A 406  HOH A 581                    
SITE     2 AC5  6 HOH B 571  HOH B 623                                          
SITE     1 AC6  3 ALA A 205  ARG A 257  GOL A 405                               
SITE     1 AC7  2 PRO A  24  HOH A 505                                          
SITE     1 AC8 12 TYR B  38  GLY B  90  GLY B  91  SER B 162                    
SITE     2 AC8 12 ALA B 163  LEU B 193  LEU B 212  ILE B 217                    
SITE     3 AC8 12 PHE B 220  HIS B 284  SER B 285  HOH B 509                    
SITE     1 AC9  3 ARG B 257  ARG B 261  HOH B 511                               
SITE     1 AD1  8 LEU B 193  ASP B 196  ALA B 197  VAL B 198                    
SITE     2 AD1  8 ASP B 221  ARG B 228  PHE B 234  HOH B 509                    
SITE     1 AD2  9 TYR C  38  LEU C  41  GLY C  90  GLY C  91                    
SITE     2 AD2  9 SER C 162  ALA C 163  LEU C 212  HIS C 284                    
SITE     3 AD2  9 SER C 285                                                     
SITE     1 AD3  4 ASP C 119  TYR C 120  HOH C 506  HOH C 591                    
SITE     1 AD4  9 TYR D  38  GLY D  90  GLY D  91  SER D 162                    
SITE     2 AD4  9 ALA D 163  LEU D 212  PHE D 220  HIS D 284                    
SITE     3 AD4  9 SER D 285                                                     
SITE     1 AD5  3 ARG D  75  GLU D  76  SER D  77                               
SITE     1 AD6  4 HOH C 635  ARG D 257  ARG D 261  GOL D 404                    
SITE     1 AD7  4 ALA D 205  PHE D 206  ARG D 257  GOL D 403                    
SITE     1 AD8  7 LEU D 193  ASP D 196  ALA D 197  VAL D 198                    
SITE     2 AD8  7 ILE D 217  ASP D 221  ARG D 228                               
CRYST1   70.772  129.603  219.707  90.00  90.00  90.00 P 21 2 21    16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014130  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007716  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004552        0.00000                         
TER    2282      GLY A 312                                                      
TER    4560      GLY B 312                                                      
TER    6838      GLY C 312                                                      
TER    9115      GLY D 312                                                      
MASTER      443    0   17   49   32    0   31    610291    4  138  100          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
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